Amyloidogenic propensity of self-assembling peptides and their adjuvant potential for use as DNA vaccines.

ABSTRACT: De novo designed peptides that self-assemble into cross-β rich fibrillar biomaterials have been pursued as an innovative platform for the development of adjuvant- and inflammation-free vaccines. However, they share structural and morphological properties similar to amyloid species implicated in neurodegenerative diseases, which has been a long-standing concern for their successful translation. Here, we comprehensively characterize the amyloidogenic character of the amphipathic self-assembling cross-β peptide KFE₈, compared to pathological amyloid and amyloid-like proteins α-synuclein (α-syn) and TDP-43. Further, we developed plasmid-based DNA vaccines with the KFE₈ backbone serving as a scaffold for delivery of a GFP model antigen. We find that expression of tandem re

SUBMITTER: Shrimali PC 

PROVIDER: S-EPMC12516588 | biostudies-literature | 2023 Oct

REPOSITORIES: biostudies-literature